3d11

X-ray diffraction
2.31Å resolution

Crystal Structures of the Nipah G Attachment Glycoprotein

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Glycoprotein G Chain: A
Molecule details ›
Chain: A
Length: 428 amino acids
Theoretical weight: 47.97 KDa
Source organism: Nipah henipavirus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9IH62 (Residues: 176-602; Coverage: 71%)
Gene name: G
Sequence domains: Haemagglutinin-neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P213
Unit cell:
a: 130.161Å b: 130.161Å c: 130.161Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.257
Expression system: Spodoptera frugiperda